6V6H
Crystal structure of histidine ammonia-lyase from Trypanosoma cruzi
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LNLS BEAMLINE W01B-MX2 |
Synchrotron site | LNLS |
Beamline | W01B-MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-09-24 |
Detector | DECTRIS PILATUS 2M |
Wavelength(s) | 1.458 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 87.812, 144.555, 173.762 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.314 - 2.550 |
R-factor | 0.1805 |
Rwork | 0.179 |
R-free | 0.21660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gkm |
RMSD bond length | 0.003 |
RMSD bond angle | 13.213 |
Data reduction software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 111.130 | 2.630 |
High resolution limit [Å] | 2.550 | 2.550 |
Number of reflections | 72424 | 6307 |
<I/σ(I)> | 11.9 | |
Completeness [%] | 99.3 | |
Redundancy | 6 | |
CC(1/2) | 0.991 | 0.732 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291.15 | 1 mol L-1 succinic acid, 1% (w/v) PEG mme 2.000 and 0.1 mol L-1 HEPES buffer pH 7.0 |